AK1CD_MOUSE
ID AK1CD_MOUSE Reviewed; 323 AA.
AC Q8VC28; Q9D7R9; Q9R0M9;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aldo-keto reductase family 1 member C13;
DE EC=1.1.1.-;
GN Name=Akr1c13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach;
RX PubMed=10526179; DOI=10.1016/s0014-5793(99)01243-0;
RA Ikeda S., Okuda-Ashitaka E., Masu Y., Suzuki T., Watanabe K., Nakao M.,
RA Shingu K., Ito S.;
RT "Cloning and characterization of two novel aldo-keto reductases (AKR1C12
RT and AKR1C13) from mouse stomach.";
RL FEBS Lett. 459:433-437(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 201-209, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) IN COMPLEX WITH NAD.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of putative reductase (NP_038806.2) from Mus musculus at
RT 1.18 A resolution.";
RL Submitted (FEB-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the dehydrogenation of 17-beta-hydroxysteroids. May
CC also exhibit significant activity with a variety of cyclic and
CC alicyclic alcohols. Uses both NAD and NADP, but the activity is much
CC greater with NAD than with NADP (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AB027125; BAA86850.1; -; mRNA.
DR EMBL; AK008949; BAB25986.1; -; mRNA.
DR EMBL; BC021937; AAH21937.1; -; mRNA.
DR CCDS; CCDS26220.1; -.
DR RefSeq; NP_038806.2; NM_013778.2.
DR PDB; 3LN3; X-ray; 1.18 A; A=1-323.
DR PDB; 5UXF; X-ray; 1.50 A; A=1-323.
DR PDB; 6M7K; X-ray; 1.10 A; A=3-323.
DR PDBsum; 3LN3; -.
DR PDBsum; 5UXF; -.
DR PDBsum; 6M7K; -.
DR AlphaFoldDB; Q8VC28; -.
DR SMR; Q8VC28; -.
DR STRING; 10090.ENSMUSP00000021634; -.
DR iPTMnet; Q8VC28; -.
DR PhosphoSitePlus; Q8VC28; -.
DR SwissPalm; Q8VC28; -.
DR EPD; Q8VC28; -.
DR jPOST; Q8VC28; -.
DR MaxQB; Q8VC28; -.
DR PaxDb; Q8VC28; -.
DR PRIDE; Q8VC28; -.
DR ProteomicsDB; 296009; -.
DR DNASU; 27384; -.
DR Ensembl; ENSMUST00000021634; ENSMUSP00000021634; ENSMUSG00000021213.
DR GeneID; 27384; -.
DR KEGG; mmu:27384; -.
DR UCSC; uc007pjl.2; mouse.
DR CTD; 27384; -.
DR MGI; MGI:1351662; Akr1c13.
DR VEuPathDB; HostDB:ENSMUSG00000021213; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000162368; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q8VC28; -.
DR OMA; IHWPIPL; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; Q8VC28; -.
DR TreeFam; TF106492; -.
DR BioGRID-ORCS; 27384; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Akr1c13; mouse.
DR EvolutionaryTrace; Q8VC28; -.
DR PRO; PR:Q8VC28; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8VC28; protein.
DR Bgee; ENSMUSG00000021213; Expressed in epithelium of small intestine and 150 other tissues.
DR ExpressionAtlas; Q8VC28; baseline and differential.
DR Genevisible; Q8VC28; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0047020; F:15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity; ISO:MGI.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; ISO:MGI.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:MGI.
DR GO; GO:0047042; F:androsterone dehydrogenase (B-specific) activity; ISO:MGI.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; ISO:MGI.
DR GO; GO:0032052; F:bile acid binding; ISO:MGI.
DR GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
DR GO; GO:0047743; F:chlordecone reductase activity; ISO:MGI.
DR GO; GO:0047787; F:delta4-3-oxosteroid 5beta-reductase activity; ISO:MGI.
DR GO; GO:0035410; F:dihydrotestosterone 17-beta-dehydrogenase activity; ISO:MGI.
DR GO; GO:0045550; F:geranylgeranyl reductase activity; ISO:MGI.
DR GO; GO:0045703; F:ketoreductase activity; ISO:MGI.
DR GO; GO:0047086; F:ketosteroid monooxygenase activity; ISO:MGI.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; ISO:MGI.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; ISO:MGI.
DR GO; GO:0018636; F:phenanthrene 9,10-monooxygenase activity; ISO:MGI.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISO:MGI.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; ISO:MGI.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:MGI.
DR CDD; cd19108; AKR_AKR1C1-35; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044482; AKR1C.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..323
FT /note="Aldo-keto reductase family 1 member C13"
FT /id="PRO_0000124644"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 20..24
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 216..224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 270..280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.6"
FT SITE 84
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT CONFLICT 47
FT /note="R -> L (in Ref. 1; BAA86850)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="I -> V (in Ref. 3; AAH21937)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="K -> N (in Ref. 2; BAB25986)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="E -> K (in Ref. 1; BAA86850)"
FT /evidence="ECO:0000305"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:5UXF"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:6M7K"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:6M7K"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6M7K"
SQ SEQUENCE 323 AA; 37058 MW; 8B51A5820402AE5A CRC64;
MSSKQHCVKL NDGHLIPALG FGTYKPKEVP KSKSLEAACL ALDVGYRHVD TAYAYQVEEE
IGQAIQSKIK AGVVKREDLF ITTKLWCTCF RPELVKPALE KSLKKLQLDY VDLYIMHYPV
PMKSGDNDFP VNEQGKSLLD TVDFCDTWER LEECKDAGLV KSIGVSNFNH RQLERILNKP
GLKYKPVCNQ VECHLYLNQR KLLDYCESKD IVLVAYGALG TQRYKEWVDQ NSPVLLNDPV
LCDVAKKNKR SPALIALRYL IQRGIVPLAQ SFKENEMREN LQVFGFQLSP EDMKTLDGLN
KNFRYLPAEF LVDHPEYPFV EEY
